1cwv: Difference between revisions

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New page: left|200px<br /><applet load="1cwv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cwv, resolution 2.3Å" /> '''CRYSTAL STRUCTURE OF ...
 
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[[Image:1cwv.jpg|left|200px]]<br /><applet load="1cwv" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1cwv.jpg|left|200px]]<br /><applet load="1cwv" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1cwv, resolution 2.3&Aring;" />
caption="1cwv, resolution 2.3&Aring;" />
'''CRYSTAL STRUCTURE OF INVASIN: A BACTERIAL INTEGRIN-BINDING PROTEIN'''<br />
'''CRYSTAL STRUCTURE OF INVASIN: A BACTERIAL INTEGRIN-BINDING PROTEIN'''<br />


==Overview==
==Overview==
The Yersinia pseudotuberculosis invasin protein promotes bacterial entry, by binding to host cell integrins with higher affinity than natural, substrates such as fibronectin. The 2.3 angstrom crystal structure of the, invasin extracellular region reveals five domains that form a 180 angstrom, rod with structural similarities to tandem fibronectin type III domains., The integrin-binding surfaces of invasin and fibronectin include similarly, located key residues, but in the context of different folds and surface, shapes. The structures of invasin and fibronectin provide an example of, convergent evolution, in which invasin presents an optimized surface for, integrin binding, in comparison with host substrates.
The Yersinia pseudotuberculosis invasin protein promotes bacterial entry by binding to host cell integrins with higher affinity than natural substrates such as fibronectin. The 2.3 angstrom crystal structure of the invasin extracellular region reveals five domains that form a 180 angstrom rod with structural similarities to tandem fibronectin type III domains. The integrin-binding surfaces of invasin and fibronectin include similarly located key residues, but in the context of different folds and surface shapes. The structures of invasin and fibronectin provide an example of convergent evolution, in which invasin presents an optimized surface for integrin binding, in comparison with host substrates.


==About this Structure==
==About this Structure==
1CWV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Yersinia_pseudotuberculosis Yersinia pseudotuberculosis] with CIT as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CWV OCA].  
1CWV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Yersinia_pseudotuberculosis Yersinia pseudotuberculosis] with <scene name='pdbligand=CIT:'>CIT</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CWV OCA].  


==Reference==
==Reference==
Line 13: Line 13:
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Yersinia pseudotuberculosis]]
[[Category: Yersinia pseudotuberculosis]]
[[Category: Bjorkman, P.J.]]
[[Category: Bjorkman, P J.]]
[[Category: Hamburger, Z.A.]]
[[Category: Hamburger, Z A.]]
[[Category: CIT]]
[[Category: CIT]]
[[Category: integrin-binding protein]]
[[Category: integrin-binding protein]]
[[Category: inv gene]]
[[Category: inv gene]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:48:52 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:10:33 2008''

Revision as of 13:10, 21 February 2008

File:1cwv.jpg


1cwv, resolution 2.3Å

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CRYSTAL STRUCTURE OF INVASIN: A BACTERIAL INTEGRIN-BINDING PROTEIN

OverviewOverview

The Yersinia pseudotuberculosis invasin protein promotes bacterial entry by binding to host cell integrins with higher affinity than natural substrates such as fibronectin. The 2.3 angstrom crystal structure of the invasin extracellular region reveals five domains that form a 180 angstrom rod with structural similarities to tandem fibronectin type III domains. The integrin-binding surfaces of invasin and fibronectin include similarly located key residues, but in the context of different folds and surface shapes. The structures of invasin and fibronectin provide an example of convergent evolution, in which invasin presents an optimized surface for integrin binding, in comparison with host substrates.

About this StructureAbout this Structure

1CWV is a Single protein structure of sequence from Yersinia pseudotuberculosis with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of invasin: a bacterial integrin-binding protein., Hamburger ZA, Brown MS, Isberg RR, Bjorkman PJ, Science. 1999 Oct 8;286(5438):291-5. PMID:10514372

Page seeded by OCA on Thu Feb 21 12:10:33 2008

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